Analytical Data
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Gene name
SURB7
- Application
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Alternative Names
Mediator of RNA polymerase II transcription subunit 21. Mediator complex subunit 21. RNA polymerase II holoenzyme component SRB7. RNAPII complex component SRB7. hSrb7
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q13503
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Expression Region
1-144 aa
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AA Sequence
MADRLTQLQDAVNSLADQFCNAIGVLQQCGPPASFNNIQTAINKDQPANPTEEYAQLFAALIARTAKDIDVLIDSLPSEESTAALQAASLYKLEEENHEAATCLEDVVYRGDMLLEKIQSALADIAQSQLKTRSGTHSQSLPDS
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Molecular Weight
41.58 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
SURB7, a protein involved in human cellular processes, has gained attention due to its role in various physiological and pathological contexts, including cell signaling, proliferation, and differentiation. As a member of the SURB family, SURB7 plays a critical role in regulating the splicing of pre-mRNA and has been implicated in several diseases, particularly cancers, where altered splicing can lead to aberrant gene expression. Research indicates that SURB7 interacts with specific RNA-binding proteins, contributing to the modulation of spliceosomal complexes and influencing the overall splicing landscape within cells. Additionally, studies have suggested that SURB7 may have a regulatory impact on cellular responses to stress and may act as a potential biomarker for certain conditions. Understanding the structure and function of SURB7, including the development of recombinant forms of the protein, is essential for elucidating its mechanistic roles and potential therapeutic applications. By harnessing advanced techniques in molecular biology and biochemistry, researchers aim to explore the functional properties of SURB7 and its implications in disease states, paving the way for novel interventions and improved diagnostic tools. Thus, the investigation of SURB7 recombinant proteins holds promise for enhancing our understanding of post-transcriptional regulation and its impact on human health.
